Cell-wall-bound proteinase of Lactobacillus delbrueckii subsp. lactis ACA-DC 178: characterization and specificity for beta-casein

Article Abstract:

The cell-wall bound proteinase produced by Lactobacillus delbrueckii subsp. lactis ACA-DC 178 is similar to the lactococcal P(sub 1)-type proteinases, since it predominantly hydrolyzes beta-casein and alpha- and kappa-caseins to a much lesser degree. The action of the proteinase on beta-casein also liberates four main peptides from beta-casein, all located in the C-terminal part of the molecule. The crude proteinase exhibited maximum activity at pH 6.0 and at 40 degrees C.

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Functional analysis of the gene encoding immunity to lactacin F, lafI, and its use as a Lactobacillus-specific, food-grade genetic marker

Article Abstract:

The ORFZ open reading frame is the lafI gene that encodes the immunity factor for the lactacin F system is an appropriate food-grade genetic marker in Lactobacillus species. Variations in growth temperatures and antibiotic selection cause homologous recombination, resulting in a mutation in ORFZ. The mutation causes loss of immunity to lactacin F, but does not affect the production of LafX. The lafI gene is functional in heterologous hosts.

Genetic markers

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Identification and cloning of gusA, encoding a new beta-glucuronidase from Lactobacillus gasseri ADH

Article Abstract:

Researchers describe the first isolation of a beta-glucuronidase from a bacterium other than E. coli. Three open reading frames from Lactobacillus gasseri ADH contain a 597-residue protein with 39% homology to E. coli beta-glucuronidase, a putative bile salt hydrolase and a putative protein similar to MerR-type regulatory proteins.

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